1orc
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(New page: 200px<br /><applet load="1orc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1orc, resolution 1.54Å" /> '''CRO REPRESSOR INSERT...)
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Revision as of 21:00, 20 November 2007
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CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]
Overview
A rationally designed, genetically engineered, monomeric form of the Cro, protein from bacteriophage lambda has been crystallized and its structure, determined by isomorphous replacement and refined to a resolution of 1.54, A. The structure confirms the rationale of the design but, at the same, time, reveals 1-2 A shifts throughout the monomer structure relative to, the previously determined structure of the dimeric wild-type protein., These changes include a 1.6 A main-chain shift in part of the beta-sheet, region of the molecule relative to the alpha-helical region and a 1.1 A, shift of a buried phenylalanine within the core as well as a correlated, 2.2 A shift in a solvent-exposed beta-hairpin. The conformational, adjustments appear to reflect an inherent flexibility of the protein that, is associated with its DNA-binding function.
About this Structure
1ORC is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
Reference
High-resolution structure of an engineered Cro monomer shows changes in conformation relative to the native dimer., Albright RA, Mossing MC, Matthews BW, Biochemistry. 1996 Jan 23;35(3):735-42. PMID:8547253
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